sirolimus and propionaldehyde

The pduP gene encodes a propionaldehyde dehydrogenase (PduP) was investigated for the role in 3-hydroxypropionic acid (3-HP) glycerol metabolism in Klebsiella pneumoniae. The enzyme assay showed that cell extracts from a pduP mutant strain lacked measurable dehydrogenase activity. Additionally, the mutant strain accumulated the cytotoxic intermediate metabolite 3-hydroxypropionaldehyde (3-HPA), causing both cell death and a lower final 3-HP titer. Ectopic expression of pduP restored normal cell growth to mutant. The enzymatic property of recombinant protein from Escherichia coli was examined, exhibiting a broad substrate specificity, being active on 3-HPA. The present work is thus the first to demonstrate the role of PduP in glycerol metabolism and biosynthesis of 3-HP.

Topics: Aldehydes; Amino Acid Sequence; Bacterial Proteins; Biosynthetic Pathways; Escherichia coli; Gene Deletion; Klebsiella pneumoniae; Lactic Acid; Microbial Viability; Molecular Sequence Data; Oxidoreductases; Sequence Analysis, Protein; Sirolimus; Substrate Specificity